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FEMS Immunol Med Microbiol. 1995 Jan;10(2):109-14.

Some binding properties of the envelope of Porphyromonas gingivalis to hemoglobin.

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Department of Oral Microbiology, Matsumoto Dental College, Nagano-Ken, Japan.


Porphyromonas gingivalis was found to bind to hemoproteins (hemoglobin, myoglobin, catalase, cytochrome c) and the binding properties of the envelope of P. gingivalis to hemoglobin were investigated. Maximum amount of hemoglobin bound to 1 mg of the envelope was 58 micrograms. No significant binding was observed at 4 degrees C and the binding was inhibited strongly by tosyl-L-lysine chloromethyl ketone, Leupeptin, EDTA and partially by meta-periodate. Heating of the envelope at 70 degrees C for 15 min resulted in complete loss of the binding activity. The binding activity of the envelope was not influenced by the treatment with the endogenous proteases. The envelope saturated with hemoglobin could no longer bind to other hemoproteins tested, indicating that binding site for these hemoproteins are common.

[Indexed for MEDLINE]

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